Tag | Content |
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CPLM ID | CPLM-005247 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Protease HtpX |
Protein Synonyms/Alias | Heat shock protein HtpX |
Gene Name | htpX |
Gene Synonyms/Alias | b1829; JW1818 |
Created Date | July 27, 2013 |
Organism | Escherichia coli (strain K12) |
NCBI Taxa ID | 83333 |
Lysine Modification | Position | Peptide | Type | References |
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231 | HADAGSAKLVGREKM | acetylation | [1] | 281 | MTHPPLDKRIEALRT | acetylation | [1] |
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Reference | [1] Acetyl-Phosphate Is a Critical Determinant of Lysine Acetylation in E. coli. Weinert BT, Iesmantavicius V, Wagner SA, Schölz C, Gummesson B, Beli P, Nyström T, Choudhary C. Mol Cell. 2013 Jul 25;51(2):265-72. [ PMID: 23830618] |
Functional Description | Membrane-localized protease able to endoproteolytically degrade overproduced SecY but not YccA, another membrane protein. It seems to cleave SecY at specific cytoplasmic sites. Does not require ATP. Its natural substrate has not been identified. Probably plays a role in the quality control of integral membrane proteins. |
Sequence Annotation | ACT_SITE 140 140 By similarity. METAL 139 139 Zinc; catalytic (By similarity). METAL 143 143 Zinc; catalytic (By similarity). METAL 222 222 Zinc; catalytic (By similarity). |
Keyword | Autocatalytic cleavage; Cell inner membrane; Cell membrane; Complete proteome; Hydrolase; Membrane; Metal-binding; Metalloprotease; Protease; Reference proteome; Stress response; Transmembrane; Transmembrane helix; Zinc. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 293 AA |
Protein Sequence | MMRIALFLLT NLAVMVVFGL VLSLTGIQSS SVQGLMIMAL LFGFGGSFVS LLMSKWMALR 60 SVGGEVIEQP RNERERWLVN TVATQARQAG IAMPQVAIYH APDINAFATG ARRDASLVAV 120 STGLLQNMSP DEAEAVIAHE ISHIANGDMV TMTLIQGVVN TFVIFISRIL AQLAAGFMGG 180 NRDEGEESNG NPLIYFAVAT VLELVFGILA SIITMWFSRH REFHADAGSA KLVGREKMIA 240 ALQRLKTSYE PQEATSMMAL CINGKSKSLS ELFMTHPPLD KRIEALRTGE YLK 293 |
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